› 4egj

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-171882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine--D-alanine ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 334 amino acids
Theoretical weight: 35.86 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13TZ4 (Residues: 1-313; Coverage: 100%)
Gene names: Bxe_A0488, Bxeno_A3907, ddl
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P43
Unit cell:
a: 78.93Å b: 78.93Å c: 224.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.224 0.26
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

2 mentions without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)
1 more